2iba
From Proteopedia
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|PDB= 2iba |SIZE=350|CAPTION= <scene name='initialview01'>2iba</scene>, resolution 1.500Å | |PDB= 2iba |SIZE=350|CAPTION= <scene name='initialview01'>2iba</scene>, resolution 1.500Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=AZA:8-AZAXANTHINE'>AZA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Urate_oxidase Urate oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.3.3 1.7.3.3] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Urate_oxidase Urate oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.3.3 1.7.3.3] </span> |
|GENE= uaZ, uox ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5059 Aspergillus flavus]) | |GENE= uaZ, uox ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5059 Aspergillus flavus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1r51|1R51]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2iba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iba OCA], [http://www.ebi.ac.uk/pdbsum/2iba PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2iba RCSB]</span> | ||
}} | }} | ||
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[[Category: Santos, J Sopkova-de Oliveira.]] | [[Category: Santos, J Sopkova-de Oliveira.]] | ||
[[Category: h, N Colloc.]] | [[Category: h, N Colloc.]] | ||
| - | [[Category: ACE]] | ||
| - | [[Category: AZA]] | ||
| - | [[Category: NA]] | ||
[[Category: t-fold domain]] | [[Category: t-fold domain]] | ||
[[Category: tetrameric enzyme]] | [[Category: tetrameric enzyme]] | ||
[[Category: uric acid degradation]] | [[Category: uric acid degradation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:41:57 2008'' |
Revision as of 00:41, 31 March 2008
| |||||||
| , resolution 1.500Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | uaZ, uox (Aspergillus flavus) | ||||||
| Activity: | Urate oxidase, with EC number 1.7.3.3 | ||||||
| Related: | 1R51
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Urate oxidase from Aspergillus flavus complexed with its inhibitor 8-azaxanthine
Overview
In contrast with most inhalational anesthetics, the anesthetic gases xenon (Xe) and nitrous oxide (N(2)O) act by blocking the N-methyl-d-aspartate (NMDA) receptor. Using x-ray crystallography, we examined the binding characteristics of these two gases on two soluble proteins as structural models: urate oxidase, which is a prototype of a variety of intracellular globular proteins, and annexin V, which has structural and functional characteristics that allow it to be considered as a prototype for the NMDA receptor. The structure of these proteins complexed with Xe and N(2)O were determined. One N(2)O molecule or one Xe atom binds to the same main site in both proteins. A second subsite is observed for N(2)O in each case. The gas-binding sites are always hydrophobic flexible cavities buried within the monomer. Comparison of the effects of Xe and N(2)O on urate oxidase and annexin V reveals an interesting relationship with the in vivo pharmacological effects of these gases, the ratio of the gas-binding sites' volume expansion and the ratio of the narcotic potency being similar. Given these data, we propose that alterations of cytosolic globular protein functions by general anesthetics would be responsible for the early stages of anesthesia such as amnesia and hypnosis and that additional alterations of ion-channel membrane receptor functions are required for deeper effects that progress to "surgical" anesthesia.
About this Structure
2IBA is a Single protein structure of sequence from Aspergillus flavus. Full crystallographic information is available from OCA.
Reference
Protein crystallography under xenon and nitrous oxide pressure: comparison with in vivo pharmacology studies and implications for the mechanism of inhaled anesthetic action., Colloc'h N, Sopkova-de Oliveira Santos J, Retailleau P, Vivares D, Bonnete F, Langlois d'Estainto B, Gallois B, Brisson A, Risso JJ, Lemaire M, Prange T, Abraini JH, Biophys J. 2007 Jan 1;92(1):217-24. Epub 2006 Oct 6. PMID:17028130
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